Analytical Data
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Gene name
NAGA
- Application
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Alternative Names
Alpha-N-Acetylgalactosaminidase; Alpha-galactosidase B
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P17050
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Expression Region
Ile218~Gln411
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Molecular Weight
23kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
NAGA, or N-acetylgalactosamine-6-sulfatase, is an essential enzyme involved in the lysosomal degradation of glycosaminoglycans, specifically heparan sulfate and dermatan sulfate. Deficiencies in NAGA are linked to a rare genetic disorder known as Morquio A syndrome, which results in skeletal abnormalities, organ dysfunction, and reduced mobility. Research on NAGA recombinant proteins aims to provide insights into the enzyme's structure and function, as well as potential therapeutic interventions for affected individuals. By producing NAGA in a recombinant system, researchers can overcome limitations associated with natural enzyme extraction, such as low yield and potential contamination. These recombinant proteins can also serve as valuable tools for studying the enzyme's activity, substrate specificity, and interaction with other lysosomal enzymes. Furthermore, the development of recombinant NAGA may pave the way for enzyme replacement therapies, offering hope for patients with Morquio A syndrome by restoring the missing enzyme activity and improving the overall pathology associated with the disorder. This line of research not only contributes to understanding lysosomal storage disorders but also opens avenues for developing innovative treatments that enhance patients' quality of life.
